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Structural basis for LIN54 recognition of CHR elements in cell cycle-regulated promoters.


ABSTRACT: The MuvB complex recruits transcription factors to activate or repress genes with cell cycle-dependent expression patterns. MuvB contains the DNA-binding protein LIN54, which directs the complex to promoter cell cycle genes homology region (CHR) elements. Here we characterize the DNA-binding properties of LIN54 and describe the structural basis for recognition of a CHR sequence. We biochemically define the CHR consensus as TTYRAA and determine that two tandem cysteine rich regions are required for high-affinity DNA association. A crystal structure of the LIN54 DNA-binding domain in complex with a CHR sequence reveals that sequence specificity is conferred by two tyrosine residues, which insert into the minor groove of the DNA duplex. We demonstrate that this unique tyrosine-mediated DNA binding is necessary for MuvB recruitment to target promoters. Our results suggest a model in which MuvB binds near transcription start sites and plays a role in positioning downstream nucleosomes.

SUBMITTER: Marceau AH 

PROVIDER: S-EPMC4974476 | biostudies-literature | 2016 Jul

REPOSITORIES: biostudies-literature

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Structural basis for LIN54 recognition of CHR elements in cell cycle-regulated promoters.

Marceau Aimee H AH   Felthousen Jessica G JG   Goetsch Paul D PD   Iness Audra N AN   Lee Hsiau-Wei HW   Tripathi Sarvind M SM   Strome Susan S   Litovchick Larisa L   Rubin Seth M SM  

Nature communications 20160728


The MuvB complex recruits transcription factors to activate or repress genes with cell cycle-dependent expression patterns. MuvB contains the DNA-binding protein LIN54, which directs the complex to promoter cell cycle genes homology region (CHR) elements. Here we characterize the DNA-binding properties of LIN54 and describe the structural basis for recognition of a CHR sequence. We biochemically define the CHR consensus as TTYRAA and determine that two tandem cysteine rich regions are required f  ...[more]

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